标题： 低能路径用于可重复的体内蛋白质折叠 显示英文标题

标题： Low energy pathways for reproducible in vivo protein folding

摘要： 两种蛋白质被选中以测试蛋白质折叠的动能机制，其中一种属于主要的α类，另一种属于α/β类。应用靶向分子动力学来生成这两种蛋白质的折叠路径，起始于两个明确的初始构象：一个完全伸展的构象和一个α-螺旋构象。结果表明，对于这两种蛋白质，α-螺旋初始构象提供了总体较低能量的到达天然状态的路径。对于α/β蛋白，从初始α-螺旋（完全伸展）结构出发的路径中有30%（40%）导致无纠缠的天然折叠，通过引入一个明确的中间结构，成功率可以提高到85%。这些结果在结尾处详细说明了为解决蛋白质折叠问题开辟了一个新的方向。 显示英文摘要

摘要： Two proteins, one belonging to the mainly alpha class and the other belonging to the alpha/beta class, are selected to test a kinetic mechanism for protein folding. Targeted molecular dynamics is applied to generate folding pathways for those two proteins, starting from two well defined initial conformations: a fully extended and a alpha-helical conformation. The results show that for both proteins the alpha-helical initial conformation provides overall lower energy pathways to the native state. For the alpha/beta protein, 30 % (40%) of the pathways from an initial alpha-helix (fully extended) structure lead to unentangled native folds, a success rate that can be increased to 85 % by the introduction of a well-defined intermediate structure. These results open up a new direction in which to look for a solution to the protein folding problem, as detailed at the end.